Trinity-X Peptide

Compound Class and Structure Trinity-X (GLP3-RT) is a synthetic single-chain peptide of 39 amino acids, supplied as a lyophilized solid for in vitro and preclinical laboratory research. Its sequence sits within the glucagon–secretin peptide superfamily, a family in which a conserved N-terminal segment drives receptor engagement while the central helical region and C-terminal extension govern selectivity, conformational stability and plasma residence. Engineering across all three regions, together with a fatty-acid modification that supports reversible albumin association, is intended to hold one defined tri-receptor activity profile inside a single molecule instead of requiring three separate agonist peptides in the same experimental system. Receptor Pharmacology and Signalling Trinity-X is characterised as a tri-agonist at three class B1 G-protein-coupled receptors: the glucagon-like peptide-1 receptor (GLP-1R), the glucose-dependent insulinotropic polypeptide receptor (GIPR) and the glucagon receptor (GCGR). All three couple predominantly to Gαs, so receptor engagement is typically read out as adenylate cyclase activation and intracellular cAMP accumulation, followed by protein kinase A activity, CREB phosphorylation and, in β-cell systems, downstream calcium flux. Secondary signalling branches examined in vitro include β-arrestin recruitment, receptor internalisation and recycling kinetics, and biased-signalling comparisons between the three receptor arms. Because relative